ID RPOC2_NOSP7 Reviewed; 1349 AA.
AC B2J1A0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324}; OrderedLocusNames=Npun_F4987;
OS Nostoc punctiforme (strain ATCC 29133 / PCC 73102).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=63737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29133 / PCC 73102;
RX PubMed=23463784; DOI=10.1104/pp.112.213116;
RA Ekman M., Picossi S., Campbell E.L., Meeks J.C., Flores E.;
RT "A Nostoc punctiforme Sugar Transporter Necessary to Establish a
RT Cyanobacterium-Plant Symbiosis.";
RL Plant Physiol. 161:1984-1992(2013).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01324}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
CC -!- SUBUNIT: In cyanobacteria the RNAP catalytic core is composed of 2
CC alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC factor is associated with the core the holoenzyme is formed, which can
CC initiate transcription. {ECO:0000255|HAMAP-Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; CP001037; ACC83331.1; -; Genomic_DNA.
DR RefSeq; WP_012411286.1; NC_010628.1.
DR AlphaFoldDB; B2J1A0; -.
DR SMR; B2J1A0; -.
DR STRING; 63737.Npun_F4987; -.
DR EnsemblBacteria; ACC83331; ACC83331; Npun_F4987.
DR KEGG; npu:Npun_F4987; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OrthoDB; 9815296at2; -.
DR PhylomeDB; B2J1A0; -.
DR Proteomes; UP000001191; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR NCBIfam; TIGR02388; rpoC2_cyan; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 1.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..1349
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353523"
FT REGION 1298..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1349
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 293
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 300
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1349 AA; 146861 MW; 6D5F42903199A739 CRC64;
MTNEKMIFRN RVVDKGQLRN LISWAFTNYG TARTAVMADK LKDLGFRYAT KAGVSISVDD
LMIPPTKRLL LEAAEEEIRA TETRYQRGEI TEVERFQKVI DTWNGTSEAL KDEVVVHFKK
TNPLNSVYMM AFSGARGNIS QVRQLVGMRG LMADPQGEII DLPIKTNFRE GLTVTEYIIS
SYGARKGLVD TALRTADSGY LTRRLVDVSQ DVIIREFDCG TTRGLTIGPM TEGAKTLIPL
ATRLMGRVIG EDVVHPVTKE LIAARNSPIP EDLAKKIEKS GVGEVVVRSP LTCEAARSVC
QHCYGWSLAH AKMVDLGEAV GIIAAQSIGE PGTQLTMRTF HTGGVFTGEV AQQVRSKIDG
TVKLPRKLKT RTYRTRHGED ALYVEANGIM LLEPTKVGDV TPENQEVHLT QGSTLYVFDG
NKVKQGQLLA EVALGGRTTR TNTEKAVKDV ASDLAGEVQF AEVVPEQKTD RQGNTTTTAA
RGGLIWILSG EVYNLPPGAE LVVKNGDAIA ANGVLAETKL ASLHGGVVRL PEATPGKSTR
EIEIITASVV LDQATVTVQS SQGRNNYLVS TGNNQVFNLR ATPGTKVQNG QVVAELIDDR
YRTTTGGFLK FAGVEVQKKG KAKLGYEVVQ GGTLLWIPEE SHEVNKDISL LLVEDGQFVE
AGTEVVKDIF CQNSGVVEVT QKNDILREVV VKPGELLMVD DPESVIGRDN TFIQPGEEFQ
GNVATELRYI QYVETPEGPA LLSRPVVEFA VPDNPDVPST TSVSQQTGRS IQLRAVQRLP
YKDSERVKSV EGVELLRTQL VLEIEQEGEQ DHNASPLAAD IELVEDTENP EVQRLQLVIL
ESLVIRRDIT ADATQGSTQT TLEVYDGLTI APGSVVARTQ ILCKEGGEVR GVRKGTENVR
RCLVLRDVDR LTINTSTQPK VKVGDLLVEG TEVAPGVFAP ESGQVVDIKN AAAASGGESA
LSTKNYVITT RIGRPYRVSP GAVLQIEDGD LVQRGDNLVL LVFERAKTGD IIQGLPRIEE
LLEARKPKEA CILCRRGGEV KVVYAESGDE AIAIKVVESN GVVTDYPLGP GQNLIVPDGS
IVLAGQPLTD GPSNPHEILE IFFSLGSEDG IYACASLALQ KVQTFLVNEV QMVYQSQGID
ISDKHIEVIV RQMTNKVRID DGGDTTMLPG ELVELRQVEQ VNEAMAITGG ARAQYTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGYNTYE
EPGAIDDYAA EISSSVLDEV DDPLDMVLDD RTARTYNLDS PTLGESGFGS RRAERSVLDD
EDELIADEVV DDDDFEEEEE DDEDDFDDE
//
